Neurochemical Research

, Volume 34, Issue 10, pp 1838–1846

Modulation of α-Synuclein Aggregation by Dopamine: A Review

Authors

  • Su Ling Leong
    • Department of Pathology, Bio21 Molecular Science and Biotechnology InstituteThe University of Melbourne
    • The Mental Health Research Institute
  • Roberto Cappai
    • Department of Pathology, Bio21 Molecular Science and Biotechnology InstituteThe University of Melbourne
  • Kevin Jeffrey Barnham
    • Department of Pathology, Bio21 Molecular Science and Biotechnology InstituteThe University of Melbourne
    • The Mental Health Research Institute
    • Department of Pathology, Bio21 Molecular Science and Biotechnology InstituteThe University of Melbourne
    • The Mental Health Research Institute
Review Article

DOI: 10.1007/s11064-009-9986-8

Cite this article as:
Leong, S.L., Cappai, R., Barnham, K.J. et al. Neurochem Res (2009) 34: 1838. doi:10.1007/s11064-009-9986-8

Abstract

Parkinson’s disease (PD) is a progressive neurodegenerative disorder that is characterized by (1) the selective loss of dopaminergic neurons in the substantia nigra and (2) the deposition of misfolded α-synuclein (α-syn) as amyloid fibrils in the intracellular Lewy bodies in various region of the brain. Current thinking suggests that an interaction between α-syn and dopamine (DA) leads to the selective death of neuronal cells and the accumulation of misfolded α-syn. However, the exact mechanism by which this occurs is not fully defined. DA oxidation could play a key role is the pathogenesis of PD by causing oxidative stress, mitochondria dysfunction and impairment of protein metabolism. Here, we review the literature on the role of DA and its oxidative intermediates in modulating the aggregation pathways of α-syn.

Keywords

α-synucleinDopamineParkinson’s diseaseOligomersAmyloid fibrils

Copyright information

© Springer Science+Business Media, LLC 2009